A structural view of coronavirus-receptor interactions.

Area of Science:

• Virology
• Structural Biology
• Immunology

Background:

• The coronavirus (CoV) spike (S) glycoprotein mediates viral entry into host cells and transmission.
• Receptor-binding domains (RBD) within the S glycoprotein are crucial for host cell recognition and are targets for neutralizing antibodies.
• Coronaviruses utilize various cell surface molecules, particularly ectoenzymes, for cell entry.

Purpose of the Study:

• To review and analyze reported CoV-receptor complex structures.
• To highlight common features, distinct recognition modes, and determinants of binding specificity in CoV RBD.
• To understand the evolution and host adaptation of coronaviruses based on structural insights.

Main Methods:

• Review of existing crystal structures of CoV-receptor complexes.
• Comparative analysis of RBD folding and receptor recognition mechanisms.
• Examination of structural determinants of binding specificity.

Main Results:

• Structural studies reveal diverse but common features in CoV RBD recognition of cell entry receptors.
• Key determinants of binding specificity and evolution of receptor recognition modes are identified.
• RBDs of recent outbreak CoVs possess specialized platforms for cross-species receptor recognition.

Conclusions:

• Structural data provides a basis for understanding CoV receptor recognition diversity, evolution, and host adaptation.
• The specialized RBD platforms facilitate cross-species transmission and adaptation of CoVs to new hosts, including humans.